Linked Life Data

15331629

Source:http://linkedlifedata.com/resource/pubmed/id/15331629

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 20
pubmed:dateCreated
2004-9-16
pubmed:abstractText
Invasion of stromal host cells, such as myofibroblasts, into the epithelial cancer compartment may precede epithelial cancer invasion into the stroma. We investigated how colon cancer-derived myofibroblasts invade extracellular matrices in vitro in the presence of colon cancer cells. Myofibroblast spheroids invade collagen type I in a stellate pattern to form a dendritic network of extensions upon co-culture with HCT-8/E11 colon cancer cells. Single myofibroblasts also invade Matrigel trade mark when stimulated by HCT-8/E11 colon cancer cells. The confrontation of cancer cells with extracellular matrices and myofibroblasts, showed that cancer-cell-derived transforming growth factor-beta (TGF-beta) is required and sufficient for invasion of myofibroblasts. In myofibroblasts, N-cadherin expressed at the tips of filopodia is upregulated by TGF-beta. Functional N-cadherin activity is implicated in TGF-beta stimulated invasion as evidenced by the neutralizing anti-N-cadherin monoclonal antibody (GC-4 mAb), and specific N-cadherin knock-down by short interference RNA (siRNA). TGF-beta1 stimulates Jun N-terminal kinase (also known as stress-activated protein kinase) (JNK) activity in myofibroblasts. Pharmacological inhibition of JNK alleviates TGF-beta stimulated invasion, N-cadherin expression and wound healing migration. Neutralization of N-cadherin activity by the GC-4 or by a 10-mer N-cadherin peptide or by siRNA reduces directional migration, filopodia formation, polarization and Golgi-complex reorientation during wound healing. Taken together, our study identifies a new mechanism in which cancer cells contribute to the coordination of invasion of stromal myofibroblasts.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
117
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4691-703
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:15331629-Animals, pubmed-meshheading:15331629-Antigens, CD, pubmed-meshheading:15331629-Cadherins, pubmed-meshheading:15331629-Cell Adhesion Molecules, pubmed-meshheading:15331629-Cell Line, pubmed-meshheading:15331629-Cell Movement, pubmed-meshheading:15331629-Cell Polarity, pubmed-meshheading:15331629-Coculture Techniques, pubmed-meshheading:15331629-Colonic Neoplasms, pubmed-meshheading:15331629-Culture Media, Conditioned, pubmed-meshheading:15331629-Fibroblasts, pubmed-meshheading:15331629-Humans, pubmed-meshheading:15331629-Mitogen-Activated Protein Kinases, pubmed-meshheading:15331629-Muscle Cells, pubmed-meshheading:15331629-Neoplasm Invasiveness, pubmed-meshheading:15331629-Phenotype, pubmed-meshheading:15331629-Rats, pubmed-meshheading:15331629-Spheroids, Cellular, pubmed-meshheading:15331629-Transforming Growth Factor beta, pubmed-meshheading:15331629-Transforming Growth Factor beta1
pubmed:year
2004
pubmed:articleTitle
Critical role of N-cadherin in myofibroblast invasion and migration in vitro stimulated by colon-cancer-cell-derived TGF-beta or wounding.
pubmed:affiliation
Laboratory of Experimental Cancerology, Department of Radiotherapy and Nuclear Medicine, Ghent University Hospital, De Pintelaan 185, 9000 Gent, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't